Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death

p53-dependent apoptosis modulates the cytotoxicity of anticancer agents

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Apoptosis. Its significance in cancer and cancer Therapy

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Galectins. Structure and function of a large family of animal lectins.

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Apoptosis in cancer therapy: Crossing the threshold

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Galectins: A family of animal β-galactoside-binding lectins

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Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5

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Apoptosis of T cells mediated by galectin-1

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Leukocyte rolling and extravasation are severely compromised in P selectin-deficient mice

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p53-Dependent apoptosis suppresses tumor growth and progression in vivo

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Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives.

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Expression of galectin-3 modulates T-cell growth and apoptosis.

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P53, cell cycle control and apoptosis: Implications for cancer

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Galectins: A Family of Animal Lectins That Decipher Glycocodes

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Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages.

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Identification of galectin-3 as a factor in pre-mRNA splicing.

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GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM

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Bifunctional properties of lectins: lectins redefined

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Galectin-3 promotes adhesion of human neutrophils to laminin

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Structure and function of the pentraxins

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Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials.

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Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides.

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Galectin-1, an Endogenous Lectin Produced by Thymic Epithelial Cells, Induces Apoptosis of Human Thymocytes

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Inhibition of Spontaneous Metastasis in a Rat Prostate Cancer Model by Oral Administration of Modified Citrus Pectin

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Galectin-3 Is a Novel Substrate for Human Matrix Metalloproteinases-2 and -9

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Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin.

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Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells.

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Endogenous lectins from cultured cells: nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts.

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GMP-140 binds to a glycoprotein receptor on human neutrophils: evidence for a lectin-like interaction.

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Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator

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Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma.

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Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides

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A new pathway for protein export in Saccharomyces cerevisiae.

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Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis

Offner, H., Celnik, B., Bringman, T. S., Casentini-Borocz, D., Nedwin, G. E., & Vandenbark, A. A. (1990) · Journal of Neuroimmunology · doi:10.1016/0165-5728(90)90032-i · Cited by 200

Secretion of the Baby Hamster Kidney 30-kDa Galactose-Binding Lectin from Polarized and Nonpolarized Cells: A Pathway Independent of the Endoplasmic Reticulum-Golgi Complex

Sato, S., Burdett, I., & Hughes, R. C. (1993) · Experimental Cell Research · doi:10.1006/excr.1993.1157 · Cited by 199

Functional evidence that cell surface galectin-3 mediates homotypic cell adhesion.

Inohara, H., & Raz, A. (1995) · PubMed · Cited by 193

The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites

Mey, A., Leffler, H., Hmama, Z., Normier, G., & Revillard, J. P. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.4.1572 · Cited by 167

Adhesion Molecules-Their Role in Health and Disease

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Biphasic modulation of cell growth by recombinant human galectin-1

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Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism

Mahanthappa, N. K., Cooper, D. N. W., Barondes, S. H., & Schwarting, G. A. (1994) · Development · doi:10.1242/dev.120.6.1373 · Cited by 144

Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells.

Ohannesian, D. W., Lotan, D., Thomas, P., Jessup, J. M., Fukuda, M., Gabius, H., & Lotan, R. (1995) · PubMed · Cited by 144

Expression of galectins on microvessel endothelial cells and their involvement in tumour cell adhesion

Lotan, R., Belloni, P., Tressler, R., Lotan, D., Xu, X.-C., & Nicolson, G. L. (1994) · Glycoconjugate Journal · doi:10.1007/bf00731282 · Cited by 139

Human T lymphotropic virus-I infection of human T lymphocytes induces expression of the beta-galactoside-binding lectin, galectin-3.

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Synthesis of an endogeneous lectin, galectin-1, by human endothelial cells is up-regulated by endothelial cell activation

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Galectin-3 expression and effects on cyst enlargement and tubulogenesis in kidney epithelial MDCK cells cultured in three-dimensional matrices in vitro

Bao, Q., & Hughes, R. C. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.8.2791 · Cited by 117

The selectin family of carbohydrate‐binding proteins: Structure and importance of carbohydrate ligands for cell adhesion

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Apoptosis and metastasis: a superior resistance of metastatic cancer cells to programmed cell death

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An endogenous lectin, galectin-3 (ϵBP / Mac-2), potentiates IL-1 production by human monocytes

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Stimulation of vascular cell proliferation by β‐galactoside specific lectins

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Introduction to Galectins.

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S-type mammalian lectins in allergic inflammation

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The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin

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p53 prevents maturation to the CD4+CD8+ stage of thymocyte differentiation in the absence of T cell receptor rearrangement.

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Glycosyltransferase mutants: key to new insights in glycobiology

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Galectin-3, a beta-galactoside-binding animal lectin, is a marker of anaplastic large-cell lymphoma.

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Extensive amino acid sequence homologies between animal lectins.

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Galectin-3 Is a Nuclear Matrix Protein Which Binds RNA

Wang, L., Inohara, H., Pienta, K. J., & Raz, A. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2777 · Cited by 86

Carbohydrate-deficient Glycoprotein Syndrome Type II. An Autosomal Recessive N-acetylglucosaminyltransferase II Deficiency Different from Typical Hereditary Erythroblastic Multinuclearity, with a Positive Acidified-serum Lysis Test (HEMPAS)

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Apoptosis: Pathophysiology of Programmed Cell Death

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Overexpression of a β-galactoside binding protein causes transformation of BALB3T3 fibroblast cells

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LAMP-1 in cho cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin

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Expression of galectin‐1 in normal human thyroid gland and in differentiated and poorly differentiated thyroid tumors

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N-linked oligosaccharide processing and tumor cell biology.

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Commentary soluble vertebrate lectins: Ubiquitous but inscrutable proteins

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Cell-Specific Transcriptional Regulation and Reactivation of Galectin-1 Gene Expression Are Controlled by DNA Methylation of the Promoter Region

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The second intron of the human galectin‐3 gene has a strong promoter activity down‐regulated by p53

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Identification of cells expressing galectin‐1, a galactose‐binding receptor, in the rat olfactory system

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Growth-associated glycosylation of transferrin secreted by HepG2 cells.

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Expression of the endogenous 14-kDa ?-galactoside-binding lectin galectin in normal human skin

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Terminal glycosyltransferase activity: a selective role in cell adhesion

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Role of TCR specificity in CD4 versus CD8 lineage commitment.

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Role of laminin carbohydrates on cellular interactions

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Activation of the galectin-1 (L-14-I) gene from nonexpressing differentiated cells by fusion with undifferentiated and tumorigenic cells.

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Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases

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Protein glycosylation in development and disease

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